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5HTB

Crystal structure of haspin (GSG2) in complex with bisubstrate inhibitor ARC-3353

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MRD A 801
ChainResidue
APRO571
AILE698
AHOH1023

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 802
ChainResidue
AGLU554
APHE556
AGLU606
AHOH907
AHOH1116
AHOH1138

site_idAC3
Number of Residues4
Detailsbinding site for residue DMS A 803
ChainResidue
ATYR667
ALYS672
ASER674
AHOH945

site_idAC4
Number of Residues28
Detailsbinding site for residue 6L5 B 101
ChainResidue
AILE490
AGLY491
AGLU492
AGLY493
AVAL494
APHE495
AGLY496
AALA509
AILE557
AGLU606
APHE607
AGLY608
AGLY609
AASP611
AGLY653
ALEU656
AILE686
ATHR689
AHOH929
AHOH944
AHOH985
AHOH1022
BMPD102
BHOH203
BHOH204
BHOH207
BHOH208
BHOH212

site_idAC5
Number of Residues2
Detailsbinding site for residue MPD B 102
ChainResidue
ATHR689
B6L5101

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGVFGEVFqTiadhtp............VAIK
ChainResidueDetails
AILE490-LYS511

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP649

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE490
ALYS511

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19918057, ECO:0007744|PDB:3DLZ
ChainResidueDetails
AGLU606
AASP649

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19918057
ChainResidueDetails
AASP687

219140

PDB entries from 2024-05-01

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